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Database: UniProt
Entry: A0A0Q7EIC7_9CAUL
LinkDB: A0A0Q7EIC7_9CAUL
Original site: A0A0Q7EIC7_9CAUL 
ID   A0A0Q7EIC7_9CAUL        Unreviewed;       421 AA.
AC   A0A0Q7EIC7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQW82569.1};
GN   ORFNames=ASC65_10140 {ECO:0000313|EMBL:KQW82569.1};
OS   Brevundimonas sp. Root1279.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW82569.1, ECO:0000313|Proteomes:UP000050923};
RN   [1] {ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW82569.1, ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|EMBL:KQW82569.1,
RC   ECO:0000313|Proteomes:UP000050923};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQW82569.1}.
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DR   EMBL; LMEB01000006; KQW82569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7EIC7; -.
DR   STRING; 1736443.ASC65_10140; -.
DR   Proteomes; UP000050923; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050923}.
FT   DOMAIN          23..159
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          174..338
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   421 AA;  44240 MW;  A2B76A86CF26A6E0 CRC64;
     MTARLHTLSN GLRVVCDPMP GLRTLALTVA VRGGAKWEDA SRSGWSHCLE HLVFKGAGEM
     SAREIVERIE AEGGSLNAAT GYERTSFEVR ALQGSLGLAM QVVSDLVFRP TLDPDEIERE
     KDVVAQEIAE AFDTPDDHVF EMAQTRAYGD QPLGRPILGS VASLKPIKRA GIGEWRARLY
     SPDRMVVSAS GAVDETELLA LAERWFGGEA ATPADAPAAP VFTGGDATLT RRIEQANVVF
     LLPAPSAVDP AYPAARLMTE ILGGGMASRL FQSAREARGL AYAIDAYHEP YEDAGLLGIY
     AGAAADRSVE LAKVCAAELK ALAEHGPTDV ELSRSKAVLN AGLWMSDESP AARAGRAAAQ
     VLIFGAPIGS QTMADRVLAQ TAEDVRAAAA VTLSAGLAAT AVLGPKTAAP AGAAFRYALF
     A
//
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